Journal
INFLAMMATION RESEARCH
Volume 67, Issue 1, Pages 1-3Publisher
SPRINGER BASEL AG
DOI: 10.1007/s00011-017-1097-4
Keywords
Protein Kinase C; Munc18a; Mast cell degranulation; RBL-2H3; Inflammation; Phosphorylation
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Funding
- National Institute of Allergy and Infectious Diseases [R15AI133430] Funding Source: Medline
- NIAID NIH HHS [R15 AI133430] Funding Source: Medline
- NIGMS NIH HHS [P20 GM103476, P20GM103476] Funding Source: Medline
- University of Southern Mississippi [DE01407] Funding Source: Medline
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Protein Kinase C (PKC) regulates the release of pro-inflammatory compounds from IgE/antigen-activated mast cells by unknown mechanisms. In this study, we show for the first time that PKC inhibitor Ro-03-0432, which inhibits RBL-2H3 exocytosis/degranulation in a concentration-dependent fashion, prevents the phosphorylation of membrane fusion factor Munc18a at Ser 313. Our study provides fresh evidence that PKC-dependent protein phosphorylation may contribute to the intricate regulation of mast cell degranulation by directly targeting the fusion factors.
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